scholarly journals Differential Stability of Dimeric and Monomeric CytochromecOxidase Exposed to Elevated Hydrostatic Pressure†

Biochemistry ◽  
2007 ◽  
Vol 46 (24) ◽  
pp. 7146-7152 ◽  
Author(s):  
Jana Staničová ◽  
Erik Sedlák ◽  
Andrej Musatov ◽  
Neal C. Robinson
1991 ◽  
Vol 42 (7) ◽  
pp. 2063-2071 ◽  
Author(s):  
B. T. Stokke ◽  
K. D. Knudsen ◽  
O. Smidsrød ◽  
A. Elgsaeter

2000 ◽  
Vol 192 (1) ◽  
pp. 91-95 ◽  
Author(s):  
Akihiko Ikegami ◽  
Kaoru Nakasone ◽  
Chiaki Kato ◽  
Yuka Nakamura ◽  
Ikuko Yoshikawa ◽  
...  

2009 ◽  
Vol 297 (1) ◽  
pp. C111-C120 ◽  
Author(s):  
Amritlal Mandal ◽  
Mohammad Shahidullah ◽  
Nicholas A. Delamere ◽  
Marcos A. Terán

Optic nerve head astrocytes become abnormal in eyes that have elevated intraocular pressure, and cultured astrocytes display altered protein expression after being subjected for ≥1 days to elevated hydrostatic pressure. Here we show that 2-h elevated hydrostatic pressure (15 or 30 mmHg) causes phosphorylation of ERK1/2, ribosomal S6 protein kinase (p90RSK), and Na/H exchanger (NHE)1 in cultured rat optic nerve head astrocytes as judged by Western blot analysis. The MEK/ERK inhibitor U0126 abolished phosphorylation of NHE1 and p90RSK as well as ERK1/2. To examine NHE1 activity, cytoplasmic pH (pHi) was measured with BCECF and, in some experiments, cells were acidified by 5-min exposure to 20 mM ammonium chloride. Although baseline pHi was unaltered, the rate of pHi recovery from acidification was fourfold higher in pressure-treated astrocytes. In the presence of either U0126 or dimethylamiloride (DMA), an NHE inhibitor, hydrostatic pressure did not change the rate of pHi recovery. The findings are consistent with NHE1 activation due to phosphorylation of ERK1/2, p90RSK, and NHE1 that occurs in response to hydrostatic pressure. These responses may precede long-term changes of protein expression known to occur in pressure-stressed astrocytes.


Sign in / Sign up

Export Citation Format

Share Document